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Isolation, partial characterization and complete amino acid sequence of the toxic phospholipase A2 from the venom of the common viper, Vipera berus berus. 1993

I Krizaj, and J Siigur, and M Samel, and V Cotic, and F Gubensek
Department of Biochemistry, J. Stefan Institute, Ljubljana, Slovenia.

A basic, toxic phospholipase A2 was purified from the venom of Vipera berus berus (Vbb) by a single purification step, using hydrophobic chromatography. The primary structure of isolated protein was established from peptides generated by Gly-specific papaya proteinase IV, beta-trypsin, CNBr and mild acid hydrolysis. The enzyme consists of a single chain of 122 amino acid residues with 14 Cys in positions characteristic for the phospholipase A2 subgroup IIA. As far as we know, this is the first complete Vipera berus phospholipase A2 amino acid sequence reported.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010741 Phospholipases A Phospholipases that hydrolyze one of the acyl groups of phosphoglycerides or glycerophosphatidates.
D002853 Chromatography, Liquid Chromatographic techniques in which the mobile phase is a liquid. Liquid Chromatography
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D014757 Viper Venoms Venoms from SNAKES of the viperid family. They tend to be less toxic than elapid or hydrophid venoms and act mainly on the vascular system, interfering with coagulation and capillary membrane integrity and are highly cytotoxic. They contain large amounts of several enzymes, other factors, and some toxins. Russell Viper Venom,Russell Viper Venoms,Russell's Viper Venom,Russell's Viper Venoms,Viperidae Venoms,Cerastes Venom,Cerastes Venoms,Egyptian Sand Viper Venom,Viper Venom,Viperotoxin,Russells Viper Venom,Russells Viper Venoms,Venom, Cerastes,Venom, Russell Viper,Venom, Russell's Viper,Venom, Viper,Venoms, Cerastes,Venoms, Russell Viper,Venoms, Russell's Viper,Venoms, Viper,Venoms, Viperidae,Viper Venom, Russell,Viper Venom, Russell's,Viper Venoms, Russell,Viper Venoms, Russell's
D017386 Sequence Homology, Amino Acid The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species. Homologous Sequences, Amino Acid,Amino Acid Sequence Homology,Homologs, Amino Acid Sequence,Homologs, Protein Sequence,Homology, Protein Sequence,Protein Sequence Homologs,Protein Sequence Homology,Sequence Homology, Protein,Homolog, Protein Sequence,Homologies, Protein Sequence,Protein Sequence Homolog,Protein Sequence Homologies,Sequence Homolog, Protein,Sequence Homologies, Protein,Sequence Homologs, Protein
D054467 Phospholipases A2 Phospholipases that hydrolyze the acyl group attached to the 2-position of PHOSPHOGLYCERIDES. Lecithinase A2,Phospholipase A2

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